BMRB Entry 15128
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15128
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Title: Solution structure of the RGS domain of human RGS14 PubMed: 18434541
Deposition date: 2007-02-02 Original release date: 2007-08-23
Authors: Dowler, Elizabeth; Diehl, Annette; Bray, James; Elkins, Jon; Soundararajan, Meera; Doyle, Declan; Gileadi, Carina; Phillips, Claire; Schoch, Guillaume; Yang, Xiawen; Brockmann, Christoph; Leidert, Martina; Rehbein, Kristina; Schmieder, Peter; Kuhne, Ronald; Higman, Victoria; Sundstrom, Michael; Arrowsmith, Cheryl; Weigelt, Johan; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda
Citation: Soundararajan, Meera; Willard, Francis; Kimple, Adam; Turnbull, Andrew; Ball, Linda; Schoch, Guillaume; Gileadi, Carina; Fedorov, Oleg; Dowler, Elizabeth; Higman, Victoria; Hutsell, Stephanie; Sundstrom, Michael; Doyle, Declan; Siderovski, David. "Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits" Proc. Natl. Acad. Sci. USA 105, 6457-6462 (2008).
Assembly members:
RGS14, polymer, 154 residues, 17728.135 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RGS14: SMTEEQPVASWALSFERLLQ
DPLGLAYFTEFLKKEFSAEN
VTFWKACERFQQIPASDTQQ
LAQEARNIYQEFLSSQALSP
VNIDRQAWLGEEVLAEPRPD
MFRAQQLQIFNLMKFDSYAR
FVKSPLYRECLLAEAEGRPL
REPGSSRLGSPDAT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 567 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 1011 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RGS domain | 1 |
Entities:
Entity 1, RGS domain 154 residues - 17728.135 Da.
The two residues at the extreme N-terminus (SM) are from the vector following TEV cleavage of the N-terminus hexahistidine purification tag.
| 1 | SER | MET | THR | GLU | GLU | GLN | PRO | VAL | ALA | SER | ||||
| 2 | TRP | ALA | LEU | SER | PHE | GLU | ARG | LEU | LEU | GLN | ||||
| 3 | ASP | PRO | LEU | GLY | LEU | ALA | TYR | PHE | THR | GLU | ||||
| 4 | PHE | LEU | LYS | LYS | GLU | PHE | SER | ALA | GLU | ASN | ||||
| 5 | VAL | THR | PHE | TRP | LYS | ALA | CYS | GLU | ARG | PHE | ||||
| 6 | GLN | GLN | ILE | PRO | ALA | SER | ASP | THR | GLN | GLN | ||||
| 7 | LEU | ALA | GLN | GLU | ALA | ARG | ASN | ILE | TYR | GLN | ||||
| 8 | GLU | PHE | LEU | SER | SER | GLN | ALA | LEU | SER | PRO | ||||
| 9 | VAL | ASN | ILE | ASP | ARG | GLN | ALA | TRP | LEU | GLY | ||||
| 10 | GLU | GLU | VAL | LEU | ALA | GLU | PRO | ARG | PRO | ASP | ||||
| 11 | MET | PHE | ARG | ALA | GLN | GLN | LEU | GLN | ILE | PHE | ||||
| 12 | ASN | LEU | MET | LYS | PHE | ASP | SER | TYR | ALA | ARG | ||||
| 13 | PHE | VAL | LYS | SER | PRO | LEU | TYR | ARG | GLU | CYS | ||||
| 14 | LEU | LEU | ALA | GLU | ALA | GLU | GLY | ARG | PRO | LEU | ||||
| 15 | ARG | GLU | PRO | GLY | SER | SER | ARG | LEU | GLY | SER | ||||
| 16 | PRO | ASP | ALA | THR |
Samples:
sample_1: RGS14, [U-95% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; DTT, [U-99% 2H], 1 mM
sample_2: RGS14, [U-95% 13C; U-95% 15N], 1.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT, [U-99% 2H], 1 mM; D2O 10%
sample_3: RGS14, [U-95% 13C; U-95% 15N], 1.4 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT, [U-99% 2H], 1 mM; D2O 10%
sample_4: RGS14, [U-95% 13C; U-95% 15N], 1.1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT, [U-99% 2H], 1 mM; D2O, [U-100% 2H], 100%; sodium azide 0.02%
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 297 K
sample_conditions_2: pH: 6; pressure: 1 atm; temperature: 297 K
sample_conditions_3: pH: 6.2; pressure: 1 atm; temperature: 297 K
sample_conditions_4: pH: 6; pressure: 1 atm; temperature: 297 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_3 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_3 |
| 3D HCCH-COSY | sample_4 | isotropic | sample_conditions_4 |
| 3D 1H-13C HMQC NOESY | sample_4 | isotropic | sample_conditions_4 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_4 |
| 2D DQF-COSY | sample_4 | isotropic | sample_conditions_4 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_4 |
Software:
xwinnmr v2.6 and 3.1, Bruker Biospin - collection, processing
SPARKY v3.100, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.14, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DMX 750 MHz
Related Database Links:
| PDB | |
| DBJ | BAJ20688 |
| GB | AAH14094 ADZ15921 EAW85011 EAW85012 EAW85013 |
| REF | NP_001179660 NP_006471 XP_001089197 XP_002744538 XP_003280558 |
| SP | O43566 |
| TPG | DAA27643 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts